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Aggregation-resistant alpha-synuclein tetramers are reduced in the blood of Parkinson's patients. | LitMetric

AI Article Synopsis

  • - The study focuses on synucleinopathies, specifically Parkinson's disease (PD), characterized by the buildup of α-synuclein protein in the brain and other tissues.
  • - Researchers examined blood samples from familial PD patients with G51D mutations and sporadic PD patients, finding that levels of stable α-synuclein tetramers were lower compared to control groups.
  • - The decrease in α-synuclein tetramers was also observed in asymptomatic G51D carriers, suggesting that destabilization of these proteins may occur before the onset of PD symptoms, pointing to their potential use as early biomarkers for the disease.

Article Abstract

Synucleinopathies such as Parkinson's disease (PD) are defined by the accumulation and aggregation of the α-synuclein protein in neurons, glia and other tissues. We have previously shown that destabilization of α-synuclein tetramers is associated with familial PD due to SNCA mutations and demonstrated brain-region specific alterations of α-synuclein multimers in sporadic PD patients following the classical Braak spreading theory. In this study, we assessed relative levels of disordered and higher-ordered multimeric forms of cytosolic α-synuclein in blood from familial PD with G51D mutations and sporadic PD patients. We used an adapted in vitro-cross-linking protocol for human EDTA-whole blood. The relative levels of higher-ordered α-synuclein tetramers were diminished in blood from familial PD and sporadic PD patients compared to controls. Interestingly, the relative amount of α-synuclein tetramers was already decreased in asymptomatic G51D carriers, supporting the hypothesis that α-synuclein multimer destabilization precedes the development of clinical PD. Our data, therefore suggest that measuring α-synuclein tetramers in blood may have potential as a facile biomarker assay for early detection and quantitative tracking of PD progression.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11250827PMC
http://dx.doi.org/10.1038/s44321-024-00083-5DOI Listing

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